Professor Fry’s group at the University of Leicester is focused on studying how cells divide. They want to fully understand how this process is controlled in normal cells and how it goes wrong in cancer. Ultimately they want to learn how to use drugs aimed at disturbing this process to more effectively destroy cancer cells, whilst causing the fewest side-effects for patients.

This work has produced two papers published in the same issue of the world-leading Journal of Cell Biology. Both papers suggest that a new understanding of how cells divide can reveal new targets for cancer therapy.

Two papers? So was work funded twice?

It might sound odd that two papers were both sent to the same journal, at the same time, by the same researcher. Rest assured it does not mean that work was duplicated. If there are two pieces of work that are very similar or relate to each other, it is quite common that research groups will send these results together. This provides a more complete picture and stronger evidence that what they have found can be repeated and is genuine.

What did the two papers actually show?

Professor Fry said:

Together, these two papers provide exciting new insights into how cells ensure that they faithfully pass on the right amount of genetic material to their offspring when they divide. They also reveal potential new targets for the development of novel cancer treatments.

The first of these two papers, featuring work led by Dr Laura O’Regan, shows that an enzyme called Nek6 controls the stability of the structural scaffold (stained green in the picture above) upon which the genetic material, stored in chromosomes (blue), is separated.

The team showed that Nek6 leads to recruitment of a chaperone called Hsp70 onto this scaffold. Imagine a coat done up with lots of Velcro pieces: Nek6 and Hsp70 would control the coat, and the Velcro would be the chromosomes holding the genetic material. Cell division would be like pulling the coat apart at the Velcro and ripping it from top to bottom at the back, leaving you with two identical halves.

Chaperones like Hsp70 are proteins that act as guardians inside a cell. They fold proteins into their correct shape and assemble them into fully functional groups. In the context of cancer, chaperones are ‘baddies’ and work to protect cancer cells against the stressful environment of a tumour, and actually keep them alive.

Not surprisingly then, drug companies are increasingly interested in making chaperone inhibitors as new anticancer therapies. These are drugs that turn off chaperones, and cause the cancer cells to die. The findings in this paper will help identify how best to use these new drugs to selectively kill cancer cells.

In the second paper, work led by Dr Suzanna Prosser showed that Nek5, an enzyme very similar to Nek6, also has a key role in building the structural scaffold needed for cell division. Without Nek5 genes would be damaged. To go back to the earlier analogy, Nek5 also has a role in controlling the ‘coat’, and without it the Velcro does not get done up or pulled apart correctly. This means that the coat cannot rip correctly, so the two halves are not identical.

How important are these findings, and what does it mean for patients?

Dr Helen Rippon, Head of Research at Worldwide Cancer Research, said: “There is still so much we don’t understand about how our cells grow and divide and what goes wrong to cause cancer. These findings are a great step forward, and early-stage research like this is vital if we are going to continue making the huge advances in cancer treatments we’ve already seen over the last few decades.”

Professor Fry’s Worldwide Cancer Research grant is still ongoing, and he told us “Through working with outstanding collaborators in Leicester and across the world, our future goal is to exploit this new understanding that underlies cell division to develop more effective medicines and allow better treatments for patients with a wide range of cancers in the future.”

Many thanks to Professor Andrew Fry for his microscope picture of a dividing cell.